Evidence map›Paper›PMID 21454589›Full record

ArticleThe Journal of biological chemistry2011

Lipids and topological rules of membrane protein assembly: balance between long and short range lipid-protein interactions.

Heidi Vitrac, Mikhail Bogdanov, Phil Heacock, William Dowhan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Complete topology inversion can be part of normal membrane protein biogenesis.Protein science : a publication of the Protein Society · 2017
    Article
  10. Article
  11. Article
  12. Model parameters for simulation of physiological lipids.Journal of computational chemistry · 2016
    Article
  13. Article
  14. Review
  15. Dynamic membrane protein topological switching upon changes in phospholipid environment.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. Review
  17. In vitro reconstitution of lipid-dependent dual topology and postassembly topological switching of a membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Heidi VitracDepartment of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, Texas 77030, USA.
Mikhail Bogdanov
Phil Heacock
William Dowhan
The University of Texas at Austin · US

Funding

Structure and Function in Membrane ProteinsR37GM020478 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 2005 to 2015
$5.4M
NIGMS NIH HHS GM R37 20478NIGMS NIH HHS R37 GM020478
6 · The paper itself

Abstract

The N-terminal six-transmembrane domain (TM) bundle of lactose permease of Escherichia coli is uniformly inverted when assembled in membranes lacking phosphatidylethanolamine (PE). Inversion is dependent on the net charge of cytoplasmically exposed protein domains containing positive and negative residues, net charge of the membrane surface, and low hydrophobicity of TM VII acting as a molecular hinge between the two halves of lactose permease (Bogdanov, M., Xie, J., Heacock, P., and Dowhan, W. (2008) J. Cell Biol. 182, 925-935). Net neutral lipids suppress the membrane translocation potential of negatively charged amino acids, thus increasing the cytoplasmic retention potential of positively charged amino acids. Herein, TM organization of sucrose permease (CscB) and phenylalanine permease (PheP) as a function of membrane lipid composition was investigated to extend these principles to other proteins. For CscB, topological dependence on PE only becomes evident after a significant increase in the net negative charge of the cytoplasmic surface of the N-terminal TM bundle. High negative charge is required to overcome the thermodynamic block to inversion due to the high hydrophobicity of TM VII. Increasing the positive charge of the cytoplasmic surface of the N-terminal TM hairpin of PheP, which is misoriented in PE-lacking cells, favors native orientation in the absence of PE. PheP and CscB also display co-existing dual topologies dependent on changes in the charge balance between protein domains and the membrane lipids. Therefore, the topology of both permeases is dependent on PE. However, CscB topology is governed by thermodynamic balance between opposing lipid-dependent electrostatic and hydrophobic interactions.

Indexed as

Amino Acid Transport Systems, NeutralBacterial ProteinsEscherichia coli ProteinsMembrane LipidsMembrane Transport ProteinsPhosphatidylethanolaminesAmino Acid Transport Systems, NeutralBacterial ProteinscscB protein, E coliEscherichia coli Proteinslactose permeaseMembrane LipidsMembrane Transport Proteinsphenylalanine-specific permease, E coliPhosphatidylethanolamines

Identifiers

PMID21454589
PMCPMC3083153
OpenAlexW1987198028

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.